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- 详细信息
- 文献和实验
- 技术资料
- 抗体名:
Purified anti-Tau Phospho (Thr181)
- 抗体英文名:
Purified anti-Tau Phospho (Thr181)
- 供应商:
上海善然生物科技有限公司
- 保存条件:
2-8℃
- 规格:
100ug
Purified anti-Tau Phospho (Thr181) Antibody
M7004D06
Catalog# / Size
846602 / 100 µg
Clone
Regulatory Status RUO
Other Names Microtubule associated protein tau
Isotype Mouse IgG1, κ
Description Tau protein promotes microtubule assembly and stability. Tau is abundant in neurons of the central
nervous system, and is expressed at low levels in astrocytes and oligodendrocytes. Abnormal hyperphosphorylation, aggregation, and toxic gain of function of tau is associated with several neurological
disorders, including Alzheimer’s disease (AD). The major building block of neurofibrillary lesions in AD
brains consists of paired helical filaments (PHFs) of abnormally hyperphosphorylated tau. Recent studies
indicate that cerebrospinal fluid tau phosphorylated at position threonine 181 has diagnostic utility for
several neurological disorders. Six isoforms of tau are generated by alternative splicing of the MAPT
gene. These isoforms are distinguished by the number of tubulin binding domains, 3 (3R) or 4 (4R), in the
C-terminal of the protein and by one (1N), two (2N), or no (0N) inserts in the N-terminal domain. Tau
isoforms are differentially expressed during development.
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文献和实验Determination of ERK Activity: Anti-phospho-ERK Antibodies and In Vitro Phosphorylation
The ERK signaling cascade is composed of several protein kinases that sequentially activate each other by phosphorylation. This pathway is a central component of a complex signaling network that regulates important cellular processes
Using Phospho‐Motif Antibodies to Determine Kinase Substrates
Figure 18.20.1 The specificity of phospho‐motif antibodies. HeLa cells were serum‐starved for 24 hr prior to being stimulated with 50 ng/ml IGF‐1 or 100 nM PMA for 10 min. Lysates were immunoblotted with anti‐Akt/PKB phospho‐motif (left panel
Assay of Dolichyl-Phospho-Mannose Synthase Reconstituted in a Lipid Matrix
of eukaryotic glycosyltransferases and processing glycosidases. The availability of these purified enzymes has in turn allowed determination of the crystal structures of the catalytic domains of some of the proteins, thus providing details of the active site
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